|
Name |
Accession |
Description |
Interval |
E-value |
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
1-354 |
4.94e-134 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 386.02 E-value: 4.94e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 1 MTKIAFTGGGTVGHVSVNLSLIPTALSQGYEALYIGSKNGIEREMIESQlpEIKYYPISSGKLRRYISLENAKDVFKVLK 80
Cdd:PRK00726 1 MKKILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKA--GIEFHFIPSGGLRRKGSLANLKAPFKLLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 81 GILDARKVLKKEKPDLLFSKGGFVSVPVVIAAKSLNIPTIIHESDLTPGLANKIALKFAKKIYTTFEETLNYLPKEKADF 160
Cdd:PRK00726 79 GVLQARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFKPKAVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 161 IGATIREDLKNGNAHNgyQLTGFNENKKVLLVMGGSLGSKKLNSIIRENLDALLQQYQVIHLTGKG----LKDAQVKKSG 236
Cdd:PRK00726 159 TGNPVREEILALAAPP--ARLAGREGKPTLLVVGGSQGARVLNEAVPEALALLPEALQVIHQTGKGdleeVRAAYAAGIN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 237 YIQYEFVkDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLVPLGLdQSRGDQIDNANHFADKGYAKTIDEEQLTAQIL 316
Cdd:PRK00726 237 AEVVPFI-DDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPH-AADDHQTANARALVDAGAALLIPQSDLTPEKL 314
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 612663832 317 LQELNKMEQERTRIINNMKSYEQSYTKEA---LFDKMIKDA 354
Cdd:PRK00726 315 AEKLLELLSDPERLEAMAEAARALGKPDAaerLADLIEELA 355
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-337 |
3.78e-128 |
|
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440471 [Multi-domain] Cd Length: 363 Bit Score: 371.38 E-value: 3.78e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 1 MTKIAFTGGGTVGHVSVNLSLIPTALSQGYEALYIGSKNGIEREMIESQlpEIKYYPISSGKLRRYISLENAKDVFKVLK 80
Cdd:COG0707 2 SKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAA--GYPLHTIPVGGLRRKGSLKNLKAPFRLLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 81 GILDARKVLKKEKPDLLFSKGGFVSVPVVIAAKSLNIPTIIHESDLTPGLANKIALKFAKKIYTTFEETLNYLPKEKADF 160
Cdd:COG0707 80 ALLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETKKYFPKKKAVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 161 IGATIREDLKNGNAHNGYQLTGFNENKKVLLVMGGSLGSKKLNSIIRENLDALLQQ-YQVIHLTGKGLKD------AQVK 233
Cdd:COG0707 160 TGNPVRKEILELDRPEARAKLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLEArLQVVHQTGKGDYEevraayAAAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 234 KSGYIQYEFVkDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLVPLGLdQSRGDQIDNANHFADKGYAKTIDEEQLTA 313
Cdd:COG0707 240 RPNAEVFPFI-DDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPH-AADDHQTKNARALVEAGAAVLIPQSELTP 317
|
330 340
....*....|....*....|....*..
gi 612663832 314 QILLQELNKMEQERTR---IINNMKSY 337
Cdd:COG0707 318 EKLAEALEELLEDPERlakMAEAARAL 344
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
3-335 |
6.99e-102 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340818 [Multi-domain] Cd Length: 350 Bit Score: 304.14 E-value: 6.99e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 3 KIAFTGGGTVGHVSVNLSLIPTALSQGYEALYIGSKNGIEREMIESQlpEIKYYPISSGKLRRYISLENAKDVFKVLKGI 82
Cdd:cd03785 1 KILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEA--GIPFHTIPISGLRRKGSLKNLKAPFKLLKGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 83 LDARKVLKKEKPDLLFSKGGFVSVPVVIAAKSLNIPTIIHESDLTPGLANKIALKFAKKIYTTFEETLNYLPKEKADFIG 162
Cdd:cd03785 79 RQARKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPAAKVVVTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 163 ATIREDLKNGNAHNGYQltGFNENKKVLLVMGGSLGSKKLNSIIRENLDALLQQ-YQVIHLTGKGLKDA---QVKKSG-- 236
Cdd:cd03785 159 NPVREEILNLRKELKRF--GLPPDKPTLLVFGGSQGARAINRAVPKALPKLLERgIQVIHQTGKGDYDEvkkLYEDLGin 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 237 YIQYEFVkDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLVPLGLdQSRGDQIDNANHFADKGYAKTIDEEQLTAQIL 316
Cdd:cd03785 237 VKVFPFI-DDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPY-AADDHQEANARALEKAGAAIVIDQEELTPEVL 314
|
330
....*....|....*....
gi 612663832 317 LQELNKMEQERTRiINNMK 335
Cdd:cd03785 315 AEAILDLLNDPER-LKKMA 332
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
3-339 |
2.39e-81 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT The final step of peptidoglycan subunit assembly in Escherichia coli occurs in the cytoplasm. RA Bupp K, van Heijenoort J. RL J Bacteriol 1993 Mar;175(6):1841-3 [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273460 [Multi-domain] Cd Length: 348 Bit Score: 251.82 E-value: 2.39e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 3 KIAFTGGGTVGHVSVNLSLIPTALSQGYEALYIGSKNGIEREMIESQlpEIKYYPISSGKLRRYISLENAKDVFKVLKGI 82
Cdd:TIGR01133 2 KIALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKA--GIEFYFIPVGGLRRKGSKKLLKTPLKLLKAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 83 LDARKVLKKEKPDLLFSKGGFVSVPVVIAAKSLNIPTIIHESDLTPGLANKIALKFAKKIYTTFEETLNYlpkEKADFIG 162
Cdd:TIGR01133 80 FKARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAKDH---FEAVLVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 163 ATIREDLKngNAHNGYQLTGFNENKKVLLVMGGSLGSKKLNSIIRENLDALLQQ-YQVIHLTGKG--LKDAQVKKSGYIQ 239
Cdd:TIGR01133 157 NPVRKEIR--SLPVPRERFGRREGKPTILVLGGSQGAKILNELVPKALAKLQEKgIQIVHQGGKGdlEKVKNVYQELGQE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 240 --YEFVKDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLVPlgLDQSRGDQIDNANHFADKGYAKTIDEEQLTAQILL 317
Cdd:TIGR01133 235 kiVTFIDENMAAAYAAADLVISRAGASTVAELAAAGVPAILIP--YPYAADDQYYNAKFLEDLGAGLVIRQKELLPEKLL 312
|
330 340
....*....|....*....|....*
gi 612663832 318 Q---ELNKMEQERTRIINNMKSYEQ 339
Cdd:TIGR01133 313 EallKLLLDPANLENMAEAARKLAK 337
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
4-144 |
1.13e-44 |
|
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). This N-terminal domain contains the acceptor binding site and likely membrane association site. This family also contains a large number of proteins that probably have quite distinct activities.
Pssm-ID: 427107 [Multi-domain] Cd Length: 139 Bit Score: 150.13 E-value: 1.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 4 IAFTGGGTVGHVSVNLSLIPTALSQGYEALYIGSKNGIEREMIESQlpEIKYYPISSGKLRRYISLENAKDVFKVLKGIL 83
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKA--GIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612663832 84 DARKVLKKEKPDLLFSKGGFVSVPVVIAAKSLNIPTIIHESDLTPGLANKIALKFAKKIYT 144
Cdd:pfam03033 79 KAFRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKVAP 139
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
1-354 |
4.94e-134 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 386.02 E-value: 4.94e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 1 MTKIAFTGGGTVGHVSVNLSLIPTALSQGYEALYIGSKNGIEREMIESQlpEIKYYPISSGKLRRYISLENAKDVFKVLK 80
Cdd:PRK00726 1 MKKILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKA--GIEFHFIPSGGLRRKGSLANLKAPFKLLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 81 GILDARKVLKKEKPDLLFSKGGFVSVPVVIAAKSLNIPTIIHESDLTPGLANKIALKFAKKIYTTFEETLNYLPKEKADF 160
Cdd:PRK00726 79 GVLQARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFKPKAVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 161 IGATIREDLKNGNAHNgyQLTGFNENKKVLLVMGGSLGSKKLNSIIRENLDALLQQYQVIHLTGKG----LKDAQVKKSG 236
Cdd:PRK00726 159 TGNPVREEILALAAPP--ARLAGREGKPTLLVVGGSQGARVLNEAVPEALALLPEALQVIHQTGKGdleeVRAAYAAGIN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 237 YIQYEFVkDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLVPLGLdQSRGDQIDNANHFADKGYAKTIDEEQLTAQIL 316
Cdd:PRK00726 237 AEVVPFI-DDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPH-AADDHQTANARALVDAGAALLIPQSDLTPEKL 314
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 612663832 317 LQELNKMEQERTRIINNMKSYEQSYTKEA---LFDKMIKDA 354
Cdd:PRK00726 315 AEKLLELLSDPERLEAMAEAARALGKPDAaerLADLIEELA 355
|
|
| PRK12446 |
PRK12446 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed |
1-337 |
6.99e-129 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed
Pssm-ID: 171505 [Multi-domain] Cd Length: 352 Bit Score: 373.04 E-value: 6.99e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 1 MTKIAFTGGGTVGHVSVNLSLIPTALSQGYEALYIGSKNGIEREMIESQlpEIKYYPISSGKLRRYISLENAKDVFKVLK 80
Cdd:PRK12446 1 MKKIVFTGGGSAGHVTPNLAIIPYLKEDNWDISYIGSHQGIEKTIIEKE--NIPYYSISSGKLRRYFDLKNIKDPFLVMK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 81 GILDARKVLKKEKPDLLFSKGGFVSVPVVIAAKSLNIPTIIHESDLTPGLANKIALKFAKKIYTTFEETLNYLPKEKADF 160
Cdd:PRK12446 79 GVMDAYVRIRKLKPDVIFSKGGFVSVPVVIGGWLNRVPVLLHESDMTPGLANKIALRFASKIFVTFEEAAKHLPKEKVIY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 161 IGATIREDLKNGNAHNGYQLTGFNENKKVLLVMGGSLGSKKLNSIIRENLDALLQQYQVIHLTGKGLKDAQVK-KSGYIQ 239
Cdd:PRK12446 159 TGSPVREEVLKGNREKGLAFLGFSRKKPVITIMGGSLGAKKINETVREALPELLLKYQIVHLCGKGNLDDSLQnKEGYRQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 240 YEFVKDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLVPLGLDQSRGDQIDNANHFADKGYAKTIDEEQLTAQILLQE 319
Cdd:PRK12446 239 FEYVHGELPDILAITDFVISRAGSNAIFEFLTLQKPMLLIPLSKFASRGDQILNAESFERQGYASVLYEEDVTVNSLIKH 318
|
330
....*....|....*...
gi 612663832 320 LNKMEQERTRIINNMKSY 337
Cdd:PRK12446 319 VEELSHNNEKYKTALKKY 336
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-337 |
3.78e-128 |
|
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440471 [Multi-domain] Cd Length: 363 Bit Score: 371.38 E-value: 3.78e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 1 MTKIAFTGGGTVGHVSVNLSLIPTALSQGYEALYIGSKNGIEREMIESQlpEIKYYPISSGKLRRYISLENAKDVFKVLK 80
Cdd:COG0707 2 SKRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAA--GYPLHTIPVGGLRRKGSLKNLKAPFRLLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 81 GILDARKVLKKEKPDLLFSKGGFVSVPVVIAAKSLNIPTIIHESDLTPGLANKIALKFAKKIYTTFEETLNYLPKEKADF 160
Cdd:COG0707 80 ALLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETKKYFPKKKAVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 161 IGATIREDLKNGNAHNGYQLTGFNENKKVLLVMGGSLGSKKLNSIIRENLDALLQQ-YQVIHLTGKGLKD------AQVK 233
Cdd:COG0707 160 TGNPVRKEILELDRPEARAKLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLEArLQVVHQTGKGDYEevraayAAAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 234 KSGYIQYEFVkDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLVPLGLdQSRGDQIDNANHFADKGYAKTIDEEQLTA 313
Cdd:COG0707 240 RPNAEVFPFI-DDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPH-AADDHQTKNARALVEAGAAVLIPQSELTP 317
|
330 340
....*....|....*....|....*..
gi 612663832 314 QILLQELNKMEQERTR---IINNMKSY 337
Cdd:COG0707 318 EKLAEALEELLEDPERlakMAEAARAL 344
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
3-335 |
6.99e-102 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340818 [Multi-domain] Cd Length: 350 Bit Score: 304.14 E-value: 6.99e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 3 KIAFTGGGTVGHVSVNLSLIPTALSQGYEALYIGSKNGIEREMIESQlpEIKYYPISSGKLRRYISLENAKDVFKVLKGI 82
Cdd:cd03785 1 KILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEA--GIPFHTIPISGLRRKGSLKNLKAPFKLLKGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 83 LDARKVLKKEKPDLLFSKGGFVSVPVVIAAKSLNIPTIIHESDLTPGLANKIALKFAKKIYTTFEETLNYLPKEKADFIG 162
Cdd:cd03785 79 RQARKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPAAKVVVTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 163 ATIREDLKNGNAHNGYQltGFNENKKVLLVMGGSLGSKKLNSIIRENLDALLQQ-YQVIHLTGKGLKDA---QVKKSG-- 236
Cdd:cd03785 159 NPVREEILNLRKELKRF--GLPPDKPTLLVFGGSQGARAINRAVPKALPKLLERgIQVIHQTGKGDYDEvkkLYEDLGin 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 237 YIQYEFVkDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLVPLGLdQSRGDQIDNANHFADKGYAKTIDEEQLTAQIL 316
Cdd:cd03785 237 VKVFPFI-DDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPY-AADDHQEANARALEKAGAAIVIDQEELTPEVL 314
|
330
....*....|....*....
gi 612663832 317 LQELNKMEQERTRiINNMK 335
Cdd:cd03785 315 AEAILDLLNDPER-LKKMA 332
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
3-339 |
2.39e-81 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT The final step of peptidoglycan subunit assembly in Escherichia coli occurs in the cytoplasm. RA Bupp K, van Heijenoort J. RL J Bacteriol 1993 Mar;175(6):1841-3 [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273460 [Multi-domain] Cd Length: 348 Bit Score: 251.82 E-value: 2.39e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 3 KIAFTGGGTVGHVSVNLSLIPTALSQGYEALYIGSKNGIEREMIESQlpEIKYYPISSGKLRRYISLENAKDVFKVLKGI 82
Cdd:TIGR01133 2 KIALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKA--GIEFYFIPVGGLRRKGSKKLLKTPLKLLKAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 83 LDARKVLKKEKPDLLFSKGGFVSVPVVIAAKSLNIPTIIHESDLTPGLANKIALKFAKKIYTTFEETLNYlpkEKADFIG 162
Cdd:TIGR01133 80 FKARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAKDH---FEAVLVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 163 ATIREDLKngNAHNGYQLTGFNENKKVLLVMGGSLGSKKLNSIIRENLDALLQQ-YQVIHLTGKG--LKDAQVKKSGYIQ 239
Cdd:TIGR01133 157 NPVRKEIR--SLPVPRERFGRREGKPTILVLGGSQGAKILNELVPKALAKLQEKgIQIVHQGGKGdlEKVKNVYQELGQE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 240 --YEFVKDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLVPlgLDQSRGDQIDNANHFADKGYAKTIDEEQLTAQILL 317
Cdd:TIGR01133 235 kiVTFIDENMAAAYAAADLVISRAGASTVAELAAAGVPAILIP--YPYAADDQYYNAKFLEDLGAGLVIRQKELLPEKLL 312
|
330 340
....*....|....*....|....*
gi 612663832 318 Q---ELNKMEQERTRIINNMKSYEQ 339
Cdd:TIGR01133 313 EallKLLLDPANLENMAEAARKLAK 337
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
4-144 |
1.13e-44 |
|
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). This N-terminal domain contains the acceptor binding site and likely membrane association site. This family also contains a large number of proteins that probably have quite distinct activities.
Pssm-ID: 427107 [Multi-domain] Cd Length: 139 Bit Score: 150.13 E-value: 1.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 4 IAFTGGGTVGHVSVNLSLIPTALSQGYEALYIGSKNGIEREMIESQlpEIKYYPISSGKLRRYISLENAKDVFKVLKGIL 83
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKA--GIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612663832 84 DARKVLKKEKPDLLFSKGGFVSVPVVIAAKSLNIPTIIHESDLTPGLANKIALKFAKKIYT 144
Cdd:pfam03033 79 KAFRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKVAP 139
|
|
| Glyco_tran_28_C |
pfam04101 |
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ... |
189-335 |
2.55e-24 |
|
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). Structural analysis suggests the C-terminal domain contains the UDP-GlcNAc binding site.
Pssm-ID: 427711 [Multi-domain] Cd Length: 166 Bit Score: 97.40 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 189 VLLVMGGSLGSKKLNSIIRENLDALLQQ--YQVIHLTGKGLKD---AQVKKSG--YIQYEFvKDDLTDLLAITDTVISRA 261
Cdd:pfam04101 1 TILVTGGSQGARALNELVLSVLPLLELKgeLQVLHQTGKGDLEevkIDYAELGinYEVFPF-IDNMAEYIKAADLVISRA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612663832 262 GSNAIYEFLTLRIPMLLVPLGlDQSRGDQIDNANHFADKGYAKTIDEEQLTAQILLQELNKMEQERTRIINNMK 335
Cdd:pfam04101 80 GAGTIAELLALGKPAILVPNP-SAARGHQDNNAKELVKAGAALVILQKELTPEKLIEALLKLLLNPLRLAEMAK 152
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
185-356 |
1.82e-11 |
|
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340861 [Multi-domain] Cd Length: 364 Bit Score: 64.65 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 185 ENKKVLLVMGGSLGSKKLNSIIRENLDALlQQYQVIHLTGK---------GL--KDAQVKKSGYIqyefvkDDLTDLLAI 253
Cdd:cd17507 195 PDKPTVLLMGGGGGMGPVKETVEALLDSL-RAGQVLVVCGKnkklyeklsGLeeDYINVRVLGYV------DDMNELMAA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 254 TDTVISRAGSNAIYEFLTLRIPMLLV-PLGldqsrGDQIDNANHFADKGYAKTI-DEEQLTAQILLQELNKMEQERTRii 331
Cdd:cd17507 268 SDLVITKPGGLTISEALARGLPVIIYdPIP-----GQEEENADFLENNGAGIIArDPEELLEIVARLIDPPSLLRMMS-- 340
|
170 180
....*....|....*....|....*
gi 612663832 332 NNMKSYEQSYTkealfDKMIKDALN 356
Cdd:cd17507 341 EAAKELKPPAA-----AKVIADILS 360
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
3-336 |
4.04e-09 |
|
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.
Pssm-ID: 340817 [Multi-domain] Cd Length: 404 Bit Score: 57.56 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 3 KIAFTGGGTVGHVSVNLSLIPTALSQGYEALYIGSKNGIEREMIESQLPEIKYYPISSG-------KLRRYISLENAKDV 75
Cdd:cd03784 2 RILFVPFPGQGHVNPMLPLAKALAARGHEVTVATPPFNFADLVEAAGLTFVPVGDDPDEleldsetNLGPDSLLELLRRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 76 FKVLKGILDA--RKVLKKEKPDLLFSkgGFVSVPVVIAAKSLNIPTIIH------------------ESDLTPGLANKIA 135
Cdd:cd03784 82 LKAADELLDDllAALRSSWKPDLVIA--DPFAYAGPLVAEELGIPSVRLftgpatllsaylhpfgvlNLLLSSLLEPELF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 136 LKFAKKIYTTFEETLNYLPKEKADFIGATIREDLKNGNAHNGYQLTGFNENKKVLLVMG--------------------- 194
Cdd:cd03784 160 LDPLLEVLDRLRERLGLPPFSLVLLLLRLVPPLYVIGPTFPSLPPDRPRLPSVLGGLRIvpkngplpdelwewldkqppr 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 195 -------GSLGSKKLNSIIRENLDALLQQYQ-VIHLTGKGLKDAQVKKSGYIqyeFVKDDL--TDLLA--ITDTVISRAG 262
Cdd:cd03784 240 svvyvsfGSMVRDLPEELLELIAEALASLGQrFLWVVGPDPLGGLERLPDNV---LVVKWVpqDELLAhpAVGAFVTHGG 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612663832 263 SNAIYEFLTLRIPMLLVPLGldqsrGDQIDNANHFADKGYAKTIDEEQLTAQIL---LQEL--NKMEQERTRIINNMKS 336
Cdd:cd03784 317 WNSTLEALYAGVPMVVVPLF-----ADQPNNAARVEELGAGVELDKDELTAEELakaVREVleDESYRRAAELLAELRE 390
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
92-326 |
1.51e-08 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 54.86 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 92 EKPDLLFSkgGFVSVPVVIAAKSLNIPTIIhesdLTPGlankialkfakkiytTFEETLNYLPkEKADFIGATIRedlkN 171
Cdd:COG1819 52 WRPDLVVS--DPLALAAALAAEALGIPVVS----LTPP---------------ELEYPRPPDP-ANVRFVGPLLP----D 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 172 GNAHNGYQLTGFNENKKVLLVMGGSLGSKKlnSIIRENLDALLQQ-YQVIHLTGKGLKDAQVKKSGYIQ-YEFVkdDLTD 249
Cdd:COG1819 106 GPAELPPWLEEDAGRPLVYVTLGTSANDRA--DLLRAVLEALADLgVRVVVTTGGLDPAELGPLPDNVRvVDYV--PQDA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612663832 250 LLAITDTVISRAGSNAIYEFLTLRIPMLLVPLGldqsrGDQIDNANHFADKGYAKTIDEEQLTAQILLQELNKMEQE 326
Cdd:COG1819 182 LLPRADAVVHHGGAGTTAEALRAGVPQVVVPFG-----GDQPLNAARVERLGAGLALPPRRLTAEALRAALRRLLAD 253
|
|
| PRK13608 |
PRK13608 |
diacylglycerol glucosyltransferase; Provisional |
88-356 |
2.35e-08 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 184179 [Multi-domain] Cd Length: 391 Bit Score: 55.19 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 88 VLKKEKPDLLFSKGGFVSVPVVIAAKSLNIP--TII-----HESDLTPglankialkFAKKIYTTFEETLNYL-----PK 155
Cdd:PRK13608 99 LLIKEKPDLILLTFPTPVMSVLTEQFNINIPvaTVMtdyrlHKNWITP---------YSTRYYVATKETKQDFidvgiDP 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 156 EKADFIGATIREDLKNGNAHNGYQLT-GFNENKKVLLVMGGSLG-SKKLNSIIRENLDALlQQYQVIHLTGKGLKDAQVK 233
Cdd:PRK13608 170 STVKVTGIPIDNKFETPIDQKQWLIDnNLDPDKQTILMSAGAFGvSKGFDTMITDILAKS-ANAQVVMICGKSKELKRSL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 234 KSGYIQYEFV-----KDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLvplgLDQSRGDQIDNANHFADKGYAKTIDE 308
Cdd:PRK13608 249 TAKFKSNENVlilgyTKHMNEWMASSQLMITKPGGITISEGLARCIPMIF----LNPAPGQELENALYFEEKGFGKIADT 324
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 612663832 309 EQLTAQILLqELNKMEQERTRIINNMksyEQSYTKEALFdKMIKDALN 356
Cdd:PRK13608 325 PEEAIKIVA-SLTNGNEQLTNMISTM---EQDKIKYATQ-TICRDLLD 367
|
|
| PRK13609 |
PRK13609 |
diacylglycerol glucosyltransferase; Provisional |
86-352 |
3.17e-08 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 237445 [Multi-domain] Cd Length: 380 Bit Score: 54.73 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 86 RKVLKKEKPDLLFSKGGFVSVPVVIAAKSLNIPTI-------IHESDLTPGLANK-IALKFAKKIYTTFEetlnyLPKEK 157
Cdd:PRK13609 97 KLLLQAEKPDIVINTFPIIAVPELKKQTGISIPTYnvltdfcLHKIWVHREVDRYfVATDHVKKVLVDIG-----VPPEQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 158 ADFIGATIR----EDLKNGNAHNGYQLtgfNENKKVLLVMGGSLGSKKlnsIIRENLDALLQ--QYQVIHLTGKG--LKD 229
Cdd:PRK13609 172 VVETGIPIRssfeLKINPDIIYNKYQL---CPNKKILLIMAGAHGVLG---NVKELCQSLMSvpDLQVVVVCGKNeaLKQ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 230 A----------QVKKSGYIqyefvkDDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLL---VPlgldqsrGDQIDNANH 296
Cdd:PRK13609 246 SledlqetnpdALKVFGYV------ENIDELFRVTSCMITKPGGITLSEAAALGVPVILykpVP-------GQEKENAMY 312
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 612663832 297 FADKGYAKTI-DEEQLTAQI--LLQELNKMEQERtriiNNMKSYEQSYTKEALFDKMIK 352
Cdd:PRK13609 313 FERKGAAVVIrDDEEVFAKTeaLLQDDMKLLQMK----EAMKSLYLPEPADHIVDDILA 367
|
|
| UDPGT |
pfam00201 |
UDP-glucoronosyl and UDP-glucosyl transferase; |
249-339 |
1.20e-06 |
|
UDP-glucoronosyl and UDP-glucosyl transferase;
Pssm-ID: 278624 [Multi-domain] Cd Length: 499 Bit Score: 50.10 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 249 DLLA--ITDTVISRAGSNAIYEFLTLRIPMLLVPLgldqsRGDQIDNANHFADKGYAKTIDEEQLTAQILLQELNKmeqe 326
Cdd:pfam00201 334 DLLGhpKTRAFITHAGSNGVYEAICHGVPMVGMPL-----FGDQMDNAKHMEAKGAAVTLNVLTMTSEDLLNALKE---- 404
|
90
....*....|...
gi 612663832 327 rtrIINNmKSYEQ 339
Cdd:pfam00201 405 ---VIND-PSYKE 413
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
3-194 |
1.91e-06 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.
Pssm-ID: 340837 [Multi-domain] Cd Length: 358 Bit Score: 49.13 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 3 KIAFTGGGTVGHVSVNLSLIPTALSQGYEALYIGSKNGIEREMIESQlpEIKYYPISSgkLRRYISlenakdVFKVLKGI 82
Cdd:cd03808 1 KILFIVNVDGGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDELKEL--GVKVIDIPI--LRRGIN------PLKDLKAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 83 LDARKVLKKEKPDLLF---SKGGFVSvpvVIAAKSLNIPTIIHesdLTPGLAN----------------KIALKFAKKIY 143
Cdd:cd03808 71 FKLYKLLKKEKPDIVHchtPKPGILG---RLAARLAGVPKVIY---TVHGLGFvftegkllrllyllleKLALLFTDKVI 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 612663832 144 ttfeeTLNylPKEKADFIGATIREDLK----NGNA----HNGYQLTGFNENKKVLLVMG 194
Cdd:cd03808 145 -----FVN--EDDRDLAIKKGIIKKKKtvliPGSGvdldRFQYSPESLPSEKVVFLFVA 196
|
|
| COG4671 |
COG4671 |
Predicted glycosyl transferase [General function prediction only]; |
245-334 |
2.11e-06 |
|
Predicted glycosyl transferase [General function prediction only];
Pssm-ID: 443708 [Multi-domain] Cd Length: 391 Bit Score: 49.08 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 245 DDLTDLLAITDTVISRAGSNAIYEFLTLRIPMLLVPlgLDQSRGDQIDNANHFADKGYAKTIDEEQLTAQILLQELNKM- 323
Cdd:COG4671 283 PDFEALLAAADLSVSMGGYNTVCEILSTGKPALIVP--RTAPRTEQLIRAERLAELGLVDVLHPEDLTPEALARAIAAAl 360
|
90
....*....|.
gi 612663832 324 EQERTRIINNM 334
Cdd:COG4671 361 ARPPRRSPLDL 371
|
|
| MGT |
TIGR01426 |
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) ... |
72-316 |
9.60e-06 |
|
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) subfamily of the UDP-glucuronosyltransferase family. Members include a number of glucosyl transferases for macrolide antibiotic inactivation, but also include transferases of glucose-related sugars for macrolide antibiotic production. [Cellular processes, Toxin production and resistance]
Pssm-ID: 273616 [Multi-domain] Cd Length: 392 Bit Score: 46.99 E-value: 9.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 72 AKDVFKVLKGILDArkvLKKEKPDLLFSKggFVSVPVVIAAKSLNIPTII----------HESD---LTPGLANKIA--- 135
Cdd:TIGR01426 74 LDEAEDVLPQLEEA---YKGDRPDLIVYD--IASWTGRLLARKWDVPVISsfptfaaneeFEEMvspAGEGSAEEGAiae 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 136 ----------LKFAKKIYTTFEET-----------LNYLPKE---KAD-------FIGATIREDLKNGNahngyqLTGFN 184
Cdd:TIGR01426 149 rglaeyvarlSALLEEHGITTPPVeflaaprrdlnLVYTPKAfqpAGEtfddsftFVGPCIGDRKEDGS------WERPG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612663832 185 ENKKVLLVmggSLGS--KKLNSIIRENLDALLQQ-YQVIHLTGKGLKDAQVkksGYIQYEFVKDD---LTDLLAITDTVI 258
Cdd:TIGR01426 223 DGRPVVLI---SLGTvfNNQPSFYRTCVEAFRDLdWHVVLSVGRGVDPADL---GELPPNVEVRQwvpQLEILKKADAFI 296
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 612663832 259 SRAGSNAIYEFLTLRIPMLLVPLGLDQSRgdqidNANHFADKGYAKTIDEEQLTAQIL 316
Cdd:TIGR01426 297 THGGMNSTMEALFNGVPMVAVPQGADQPM-----TARRIAELGLGRHLPPEEVTAEKL 349
|
|
| |
